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Nuclear distribution protein nudE homolog 1 (NudE)

 NDE1_HUMAN              Reviewed;         335 AA.
Q9NXR1; Q49AQ2;
13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 3.
28-MAR-2018, entry version 144.
RecName: Full=Nuclear distribution protein nudE homolog 1;
Short=NudE;
Name=NDE1; Synonyms=NUDE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=12556484; DOI=10.1128/MCB.23.4.1239-1250.2003;
Yan X., Li F., Liang Y., Shen Y., Zhao X., Huang Q., Zhu X.;
"Human Nudel and NudE as regulators of cytoplasmic dynein in poleward
protein transport along the mitotic spindle.";
Mol. Cell. Biol. 23:1239-1250(2003).
[5]
INTERACTION WITH DYNACTIN; TUBULIN GAMMA; PAFAH1B1; PCM1 AND PCNT.
PubMed=16291865; DOI=10.1091/mbc.E05-04-0360;
Guo J., Yang Z., Song W., Chen Q., Wang F., Zhang Q., Zhu X.;
"Nudel contributes to microtubule anchoring at the mother centriole
and is involved in both dynein-dependent and -independent centrosomal
protein assembly.";
Mol. Biol. Cell 17:680-689(2006).
[6]
INTERACTION WITH ZNF365, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
MUTAGENESIS OF THR-191; THR-215; THR-228; THR-243; THR-246 AND
SER-282.
PubMed=16682949; DOI=10.1038/sj.onc.1209637;
Hirohashi Y., Wang Q., Liu Q., Li B., Du X., Zhang H., Furuuchi K.,
Masuda K., Sato N., Greene M.I.;
"Centrosomal proteins Nde1 and Su48 form a complex regulated by
phosphorylation.";
Oncogene 25:6048-6055(2006).
[7]
FUNCTION, INTERACTION WITH CENPF, AND SUBCELLULAR LOCATION.
PubMed=17600710; DOI=10.1016/j.cub.2007.05.077;
Vergnolle M.A.S., Taylor S.S.;
"Cenp-F links kinetochores to Ndel1/Nde1/Lis1/dynein microtubule motor
complexes.";
Curr. Biol. 17:1173-1179(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; THR-215; THR-228;
SER-231; SER-239; THR-243; THR-246 AND SER-282, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PALMITOYLATION AT CYS-274 BY ZDHHC2; ZDHHC3 AND ZDHHC7.
PubMed=19927128; DOI=10.1038/emboj.2009.325;
Shmueli A., Segal M., Sapir T., Tsutsumi R., Noritake J., Bar A.,
Sapoznik S., Fukata Y., Orr I., Fukata M., Reiner O.;
"Ndel1 palmitoylation: a new mean to regulate cytoplasmic dynein
activity.";
EMBO J. 29:107-119(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-243; THR-246 AND
SER-282, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INVOLVEMENT IN
LIS4.
PubMed=21529752; DOI=10.1016/j.ajhg.2011.03.019;
Bakircioglu M., Carvalho O.P., Khurshid M., Cox J.J., Tuysuz B.,
Barak T., Yilmaz S., Caglayan O., Dincer A., Nicholas A.K.,
Quarrell O., Springell K., Karbani G., Malik S., Gannon C.,
Sheridan E., Crosier M., Lisgo S.N., Lindsay S., Bilguvar K.,
Gergely F., Gunel M., Woods C.G.;
"The essential role of centrosomal NDE1 in human cerebral cortex
neurogenesis.";
Am. J. Hum. Genet. 88:523-535(2011).
[13]
INVOLVEMENT IN LIS4.
PubMed=21529751; DOI=10.1016/j.ajhg.2011.04.003;
Alkuraya F.S., Cai X., Emery C., Mochida G.H., Al-Dosari M.S.,
Felie J.M., Hill R.S., Barry B.J., Partlow J.N., Gascon G.G.,
Kentab A., Jan M., Shaheen R., Feng Y., Walsh C.A.;
"Human mutations in NDE1 cause extreme microcephaly with
lissencephaly.";
Am. J. Hum. Genet. 88:536-547(2011).
[14]
ERRATUM.
Alkuraya F.S., Cai X., Emery C., Mochida G.H., Al-Dosari M.S.,
Felie J.M., Hill R.S., Barry B.J., Partlow J.N., Gascon G.G.,
Kentab A., Jan M., Shaheen R., Feng Y., Walsh C.A.;
Am. J. Hum. Genet. 88:677-677(2011).
[15]
INVOLVEMENT IN MHAC.
PubMed=22526350; DOI=10.1007/s10048-012-0326-9;
Guven A., Gunduz A., Bozoglu T.M., Yalcinkaya C., Tolun A.;
"Novel NDE1 homozygous mutation resulting in microhydranencephaly and
not microlyssencephaly.";
Neurogenetics 13:189-194(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-231; SER-239;
SER-282 AND SER-309, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Required for centrosome duplication and formation and
function of the mitotic spindle. Essential for the development of
the cerebral cortex. May regulate the production of neurons by
controlling the orientation of the mitotic spindle during division
of cortical neuronal progenitors of the proliferative ventricular
zone of the brain. Orientation of the division plane perpendicular
to the layers of the cortex gives rise to two proliferative
neuronal progenitors whereas parallel orientation of the division
plane yields one proliferative neuronal progenitor and a post-
mitotic neuron. A premature shift towards a neuronal fate within
the progenitor population may result in an overall reduction in
the final number of neurons and an increase in the number of
neurons in the deeper layers of the cortex.
{ECO:0000269|PubMed:17600710, ECO:0000269|PubMed:21529752}.
-!- SUBUNIT: Self-associates. Interacts with CNTRL, LIS1, dynein,
SLMAP and TCP1 (By similarity). Interacts with CENPF, dynactin,
tubulin gamma, PAFAH1B1, PCM1 and PCNT. Interacts with ZNF365.
{ECO:0000250, ECO:0000269|PubMed:16291865,
ECO:0000269|PubMed:16682949, ECO:0000269|PubMed:17600710}.
-!- INTERACTION:
Q70YC5:ZNF365; NbExp=4; IntAct=EBI-941227, EBI-941182;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome.
Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton,
spindle. Cleavage furrow. Note=Localizes to the interphase and S
phase centrosome. During mitosis, partially associated with the
mitotic spindle. Concentrates at the plus ends of microtubules
coincident with kinetochores in metaphase and anaphase in a CENPF-
dependent manner. Also localizes to the cleavage furrow during
cytokinesis. manner. Also localizes to the cleavage furrow during
cytokinesis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NXR1-2; Sequence=Displayed;
Name=2;
IsoId=Q9NXR1-1; Sequence=VSP_059512;
-!- TISSUE SPECIFICITY: Expressed in the neuroepithelium throughout
the developing brain, including the cerebral cortex and
cerebellum. {ECO:0000269|PubMed:21529752}.
-!- PTM: Phosphorylated in mitosis. Phosphorylated in vitro by CDC2.
Phosphorylation at Thr-246 is essential for the G2/M transition
(By similarity). {ECO:0000250}.
-!- DISEASE: Lissencephaly 4 (LIS4) [MIM:614019]: A neurodevelopmental
disorder characterized by lissencephaly, severe brain atrophy,
extreme microcephaly, and profound mental retardation.
{ECO:0000269|PubMed:21529751, ECO:0000269|PubMed:21529752}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Microhydranencephaly (MHAC) [MIM:605013]: A severe
neurodevelopmental disorder characterized by microcephaly, severe
motor and mental retardation, spasticity, and brain malformations
that include gross dilation of the ventricles with complete
absence of the cerebral hemispheres or severe delay in their
development. {ECO:0000269|PubMed:22526350}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the nudE family. {ECO:0000305}.
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EMBL; AK000108; BAA90949.1; -; mRNA.
EMBL; AC026401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF001548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001421; AAH01421.1; -; mRNA.
EMBL; BC033900; AAH33900.1; -; mRNA.
CCDS; CCDS10564.1; -. [Q9NXR1-2]
RefSeq; NP_001137451.1; NM_001143979.1. [Q9NXR1-2]
RefSeq; NP_060138.1; NM_017668.2. [Q9NXR1-2]
RefSeq; XP_016878838.1; XM_017023349.1. [Q9NXR1-1]
RefSeq; XP_016878845.1; XM_017023356.1. [Q9NXR1-1]
UniGene; Hs.655378; -.
ProteinModelPortal; Q9NXR1; -.
SMR; Q9NXR1; -.
BioGrid; 120175; 63.
IntAct; Q9NXR1; 28.
MINT; Q9NXR1; -.
STRING; 9606.ENSP00000345892; -.
iPTMnet; Q9NXR1; -.
PhosphoSitePlus; Q9NXR1; -.
SwissPalm; Q9NXR1; -.
BioMuta; NDE1; -.
DMDM; 108860813; -.
EPD; Q9NXR1; -.
MaxQB; Q9NXR1; -.
PaxDb; Q9NXR1; -.
PeptideAtlas; Q9NXR1; -.
PRIDE; Q9NXR1; -.
Ensembl; ENST00000396354; ENSP00000379642; ENSG00000072864. [Q9NXR1-2]
Ensembl; ENST00000396355; ENSP00000379643; ENSG00000072864. [Q9NXR1-2]
Ensembl; ENST00000631844; ENSP00000488199; ENSG00000275911. [Q9NXR1-2]
Ensembl; ENST00000631923; ENSP00000488050; ENSG00000275911. [Q9NXR1-2]
GeneID; 54820; -.
KEGG; hsa:54820; -.
CTD; 54820; -.
DisGeNET; 54820; -.
EuPathDB; HostDB:ENSG00000072864.12; -.
GeneCards; NDE1; -.
HGNC; HGNC:17619; NDE1.
HPA; HPA024075; -.
MalaCards; NDE1; -.
MIM; 605013; phenotype.
MIM; 609449; gene.
MIM; 614019; phenotype.
neXtProt; NX_Q9NXR1; -.
OpenTargets; ENSG00000072864; -.
Orphanet; 1665; Fetal brain disruption sequence.
Orphanet; 2177; Hydranencephaly.
Orphanet; 1083; Microlissencephaly.
PharmGKB; PA128394673; -.
eggNOG; KOG1853; Eukaryota.
eggNOG; ENOG410XPMP; LUCA.
GeneTree; ENSGT00390000000111; -.
HOGENOM; HOG000280681; -.
HOVERGEN; HBG082010; -.
InParanoid; Q9NXR1; -.
KO; K16738; -.
OMA; GIEMSNM; -.
OrthoDB; EOG091G0GBV; -.
PhylomeDB; Q9NXR1; -.
TreeFam; TF325693; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
SIGNOR; Q9NXR1; -.
ChiTaRS; NDE1; human.
GeneWiki; NDE1; -.
GenomeRNAi; 54820; -.
PRO; PR:Q9NXR1; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000072864; -.
CleanEx; HS_NDE1; -.
ExpressionAtlas; Q9NXR1; baseline and differential.
Genevisible; Q9NXR1; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0031616; C:spindle pole centrosome; ISS:UniProtKB.
GO; GO:0045202; C:synapse; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0051298; P:centrosome duplication; ISS:UniProtKB.
GO; GO:0051642; P:centrosome localization; IBA:GO_Central.
GO; GO:0021987; P:cerebral cortex development; IMP:UniProtKB.
GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0051303; P:establishment of chromosome localization; IMP:UniProtKB.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
GO; GO:0007100; P:mitotic centrosome separation; IBA:GO_Central.
GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:2000574; P:regulation of microtubule motor activity; IEA:InterPro.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
InterPro; IPR033494; NUDE.
InterPro; IPR006964; NUDE_dom.
PANTHER; PTHR10921; PTHR10921; 1.
Pfam; PF04880; NUDE_C; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell division; Centromere;
Chromosome; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Developmental protein; Differentiation; Kinetochore; Lipoprotein;
Lissencephaly; Microtubule; Mitosis; Neurogenesis; Palmitate;
Phosphoprotein; Reference proteome.
CHAIN 1 335 Nuclear distribution protein nudE homolog
1.
/FTId=PRO_0000240202.
REGION 1 93 Self-association. {ECO:0000250}.
REGION 88 156 Interaction with PAFAH1B1. {ECO:0000250}.
REGION 167 290 Interaction with CENPF. {ECO:0000250}.
COILED 18 188 {ECO:0000255}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 215 215 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 228 228 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 239 239 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 243 243 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 246 246 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 282 282 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
LIPID 274 274 S-palmitoyl cysteine; by ZDHHC2, ZDHHC3
and ZDHHC7.
{ECO:0000269|PubMed:19927128}.
VAR_SEQ 318 335 DTSCRWLSKSTTRSSSSC -> GKRLEFGKPPSHMSSSPLP
SAQGVVKMLL (in isoform 2).
/FTId=VSP_059512.
MUTAGEN 191 191 T->E: Loss of centrosomal localization
and reduced ZNF365-binding; when
associated with E-215; E-228; E-243; E-
246 and E-282.
{ECO:0000269|PubMed:16682949}.
MUTAGEN 191 191 T->V: Retained on spindle poles during
mitosis, no loss of phosphorylation in
vivo and increased ZNF365-binding; when
associated with V-215; V-228; V-243; V-
246 and A-282.
{ECO:0000269|PubMed:16682949}.
MUTAGEN 215 215 T->E: Loss of centrosomal localization
and reduced ZNF365-binding; when
associated with E-191; E-228; E-243; E-
246 and E-282.
{ECO:0000269|PubMed:16682949}.
MUTAGEN 215 215 T->V: Retained on spindle poles during
mitosis, no loss of phosphorylation in
vivo and increased ZNF365-binding; when
associated with V-191; V-228; V-243; V-
246 and A-282.
{ECO:0000269|PubMed:16682949}.
MUTAGEN 228 228 T->E: Loss of centrosomal localization
and reduced ZNF365-binding; when
associated with E-191; E-215; E-243; E-
246 and E-282.
{ECO:0000269|PubMed:16682949}.
MUTAGEN 228 228 T->V: Retained on spindle poles during
mitosis, no loss of phosphorylation in
vivo and increased ZNF365-binding; when
associated with V-191; V-215; V-243; V-
246 and A-282.
{ECO:0000269|PubMed:16682949}.
MUTAGEN 243 243 T->E: Loss of centrosomal localization
and reduced ZNF365-binding; when
associated with E-191; E-215; E-228; E-
246 and E-282.
{ECO:0000269|PubMed:16682949}.
MUTAGEN 243 243 T->V: Retained on spindle poles during
mitosis, no loss of phosphorylation in
vivo and increased ZNF365-binding; when
associated with V-191; V-215; V-228; V-
246 and A-282.
{ECO:0000269|PubMed:16682949}.
MUTAGEN 246 246 T->E: Loss of centrosomal localization
and reduced ZNF365-binding; when
associated with E-191; E-215; E-228; E-
243 and E-282.
{ECO:0000269|PubMed:16682949}.
MUTAGEN 246 246 T->V: Retained on spindle poles during
mitosis, no loss of phosphorylation in
vivo and increased ZNF365-binding; when
associated with V-191; V-215; V-228; V-
243 and A-282.
{ECO:0000269|PubMed:16682949}.
MUTAGEN 282 282 S->A: Retained on spindle poles during
mitosis, no loss of phosphorylation in
vivo and increased ZNF365-binding; when
associated with V-191; V-215; V-228; V-
243 and V-246.
{ECO:0000269|PubMed:16682949}.
MUTAGEN 282 282 S->E: Loss of centrosomal localization
and reduced ZNF365-binding; when
associated with E-191; E-215; E-228; E-
243 and E-246.
{ECO:0000269|PubMed:16682949}.
CONFLICT 191 191 T -> I (in Ref. 3; AAH33900).
{ECO:0000305}.
SEQUENCE 335 AA; 37721 MW; FC0BDD8BB90324B8 CRC64;
MEDSGKTFSS EEEEANYWKD LAMTYKQRAE NTQEELREFQ EGSREYEAEL ETQLQQIETR
NRDLLSENNR LRMELETIKE KFEVQHSEGY RQISALEDDL AQTKAIKDQL QKYIRELEQA
NDDLERAKRA TIMSLEDFEQ RLNQAIERNA FLESELDEKE NLLESVQRLK DEARDLRQEL
AVQQKQEKPR TPMPSSVEAE RTDTAVQATG SVPSTPIAHR GPSSSLNTPG SFRRGLDDST
GGTPLTPAAR ISALNIVGDL LRKVGALESK LASCRNLVYD QSPNRTGGPA SGRSSKNRDG
GERRPSSTSV PLGDKGLDTS CRWLSKSTTR SSSSC


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